A1BG_HUMAN - dbPTM
A1BG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A1BG_HUMAN
UniProt AC P04217
Protein Name Alpha-1B-glycoprotein
Gene Name A1BG
Organism Homo sapiens (Human).
Sequence Length 495
Subcellular Localization Secreted.
Protein Description
Protein Sequence MSMLVVFLLLWGVTWGPVTEAAIFYETQPSLWAESESLLKPLANVTLTCQAHLETPDFQLFKNGVAQEPVHLDSPAIKHQFLLTGDTQGRYRCRSGLSTGWTQLSKLLELTGPKSLPAPWLSMAPVSWITPGLKTTAVCRGVLRGVTFLLRREGDHEFLEVPEAQEDVEATFPVHQPGNYSCSYRTDGEGALSEPSATVTIEELAAPPPPVLMHHGESSQVLHPGNKVTLTCVAPLSGVDFQLRRGEKELLVPRSSTSPDRIFFHLNAVALGDGGHYTCRYRLHDNQNGWSGDSAPVELILSDETLPAPEFSPEPESGRALRLRCLAPLEGARFALVREDRGGRRVHRFQSPAGTEALFELHNISVADSANYSCVYVDLKPPFGGSAPSERLELHVDGPPPRPQLRATWSGAVLAGRDAVLRCEGPIPDVTFELLREGETKAVKTVRTPGAAANLELIFVGPQHAGNYRCRYRSWVPHTFESELSDPVELLVAES
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
37PhosphorylationSLWAESESLLKPLAN
CHHCCCHHHHHHHCC
48.5624719451
44N-linked_GlycosylationSLLKPLANVTLTCQA
HHHHHHCCCEEEEEE
34.6819838169
44N-linked_GlycosylationSLLKPLANVTLTCQA
HHHHHHCCCEEEEEE
34.6814760718
179N-linked_GlycosylationFPVHQPGNYSCSYRT
CCCCCCCCCEEEEEC
32.0318638581
179N-linked_GlycosylationFPVHQPGNYSCSYRT
CCCCCCCCCEEEEEC
32.0314760718
198O-linked_GlycosylationALSEPSATVTIEELA
CCCCCCEEEEHHHHC
23.63OGP
363N-linked_GlycosylationEALFELHNISVADSA
HHHHHEECCCHHHCC
40.6316335952
363N-linked_GlycosylationEALFELHNISVADSA
HHHHHEECCCHHHCC
40.6316335952
371N-linked_GlycosylationISVADSANYSCVYVD
CCHHHCCCCEEEEEE
32.9516335952
371N-linked_GlycosylationISVADSANYSCVYVD
CCHHHCCCCEEEEEE
32.9516335952

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of A1BG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of A1BG_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of A1BG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP6_HUMANABCC6physical
21988832
PRDX4_HUMANPRDX4physical
21988832
SETD7_HUMANSETD7physical
21988832
ZBT40_HUMANZBTB40physical
28514442
PSME4_HUMANPSME4physical
28514442
UBAC1_HUMANUBAC1physical
28514442
WDR62_HUMANWDR62physical
28514442
KCMF1_HUMANKCMF1physical
28514442
RN123_HUMANRNF123physical
28514442
UBR4_HUMANUBR4physical
28514442
UBXN1_HUMANUBXN1physical
28514442
ADRO_HUMANFDXRphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of A1BG_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-179; ASN-363 ANDASN-371, AND MASS SPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179, AND MASSSPECTROMETRY.
"Amino acid sequence of human plasma alpha 1B-glycoprotein: homologyto the immunoglobulin supergene family.";
Ishioka N., Takahashi N., Putnam F.W.;
Proc. Natl. Acad. Sci. U.S.A. 83:2363-2367(1986).
Cited for: PROTEIN SEQUENCE OF 22-495, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44;ASN-179; ASN-363 AND ASN-371, AND VARIANT ARG-52.

TOP